Kristen E. DeMeester

ESCAPE identifies covalent ligand-protein interactions by using prime editing to disrupt cysteine residues and assesses their impact on cellular phenotypes.

The paper identifies host proteins regulating Mycobacterium tuberculosis replication in macrophages using cysteine reactivity profiling and genetic perturbation.

The paper develops covalent ligands that specifically target a complexoform of TRMT112, revealing partner-specific functional effects through allosteric activation of METTL5.

The paper identifies inhibitors of the GRPEL1-HSPA9 chaperone complex using tryptoline stereoprobes and shows they target non-orthosteric sites.

The paper develops a chitin labeling method to study hyphal growth and homeostasis in Candida species, revealing mechanisms of morphological switching and potential antifungal targets.

The paper introduces photo-stereoprobes for expanding the ligandable proteome and demonstrates their use in discovering bioactive small molecules.

This study identifies covalent small molecules that bind FOXA1, altering its chromatin remodeling activity in prostate cancer cells.

The paper uses base editing to assess the functional impact of cysteine mutations in cancer dependency genes, identifying essential and ligandable cysteines for drug development.